Inhibition of adenosine 5′-triphosphate–creatine phosphotransferase by substrate–anion complexes. Evidence for the transition-state organization of the catalytic site

Eitemau Tebyg

• Inhibition of adenosine 5′-triphosphate–creatine phosphotransferase by substrate–anion complexes. Evidence for the transition-state organization of the catalytic site
  gan: Milner-White, E. J., et al.
  Cyhoeddwyd: (1971)
• The significance of anions in the protection by substrates of adenosine triphosphate-creatine phosphotransferase against inhibition by iodoacetamide.
  gan: Milner-White, E J, et al.
  Cyhoeddwyd: (1970)
• The conversion of adenosine 5′-phosphate into adenosine triphosphate as catalysed by adenosine triphosphate–creatine phosphotransferase and adenosine triphosphate–adenosine monophosphate phosphotransferase in the presence of phosphocreatine
  gan: Doherty, M. D., et al.
  Cyhoeddwyd: (1963)
• The mechanism of the reaction catalysed by adenosine triphosphate–creatine phosphotransferase
  gan: Morrison, J. F., et al.
  Cyhoeddwyd: (1965)
• Adenosine triphosphate–creatine phosphotransferase from ox brain: purification and isolation
  gan: Wood, T.
  Cyhoeddwyd: (1963)